The myosin-binding protein C motif binds to F-actin in a phosphorylation-sensitive manner.

@article{Shaffer2009TheMP,
  title={The myosin-binding protein C motif binds to F-actin in a phosphorylation-sensitive manner.},
  author={Justin F. Shaffer and Robert W. Kensler and Samantha P. Harris},
  journal={The Journal of biological chemistry},
  year={2009},
  volume={284 18},
  pages={12318-27}
}
Cardiac myosin-binding protein C (cMyBP-C) is a regulatory protein expressed in cardiac sarcomeres that is known to interact with myosin, titin, and actin. cMyBP-C modulates actomyosin interactions in a phosphorylation-dependent way, but it is unclear whether interactions with myosin, titin, or actin are required for these effects. Here we show using cosedimentation binding assays, that the 4 N-terminal domains of murine cMyBP-C (i.e. C0-C1-m-C2) bind to F-actin with a dissociation constant (K… CONTINUE READING
Highly Influential
This paper has highly influenced 14 other papers. REVIEW HIGHLY INFLUENTIAL CITATIONS

Citations

Publications citing this paper.
Showing 1-10 of 75 extracted citations

References

Publications referenced by this paper.

U nirsity of C alirnia, D avis on A ril 14, 2009 w w w .jb.org D ow nladed fom The cMyBP-C Motif Binds Actin

  • K. Yamamoto
  • FEBS Letters 208,
  • 1986

Similar Papers

Loading similar papers…